Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The reduction of 2,6-dichlorophenolindophenol (DCIP) was measured by amperometric methods in Morris hepatoma 3924A cells, normal isolated rat hepatocytes and in mitochondria isolated from normal rat liver. The influence of aerobic and anaerobic atmospheres and of various inhibitors of cellular metabolism, especially of the respiratory chain (KCN, NaN3, oligomycin), on DCIP-reduction were studied using glucose, succinate, beta-hydroxybutyrate, alpha-keto-glutarate and oxalacetate as substrates. Under the influence of KCN and oligomycin the velocity of DCIP-reduction was increased in both cell types. Azide showed a similar effect on tumour cells and to a lower extent on hepatocytes. Using isolated mitochondria total DCIPred was increased by KCN and azide using various mitochondrial metabolites as substrates and with ADP/Pi present. The effects of KCN, azide and oligomycin could be explained by taking DCIP as an artificial coupling site in mitochondria which is only used when oxygen is absent or when the respiratory chain is blocked by inhibitors of cytochrome oxidase. Evaluation of the reaction kinetics revealed differences between normal and transformed cells in terms of the pseudo-first-order rate constants and the activity of overall oxidoreductases. The results apparently reflect quantitative differences in enzymatic equipment and the metabolic pathways predominating in normal and neoplastic cells.
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PMID:Investigation by amperometric methods of intracellular reduction of 2,6-dichlorophenolindophenol in normal and transformed hepatocytes in the presence of different inhibitors of cellular metabolism. 229 12

White, D. C. (Rockefeller Institute, New York, N.Y.), M. P. Bryant, and D. R. Caldwell. Cytochrome-linked fermentation in Bacteroides ruminicola. J. Bacteriol. 84:822-828. 1962-Previous studies showed that Bacteroides ruminicola, an anaerobic, saccharolytic, ruminal bacterium, ferments glucose with the production of succinic, acetic, and formic acids, requires a large amount of CO(2), and most strains require heme for growth. Difference spectra of cell suspensions of both heme-requiring strain 23, B. ruminicola subsp. ruminicola, and heme-independent strain GA33, B. ruminicola subsp. brevis, showed the presence of a cytochrome (absorption maxima at 560 mmu, near 530 mmu, and 428 mmu) similar to cytochrome b. This cytochrome and flavoprotein (trough at 450 mmu) in the cells, reduced by endogenous metabolism, were oxidized on addition of air, CO(2), oxalacetate, malate, or fumarate but no oxidation occurred in the presence of succinate, malonate, lactate, pyruvate, aspartate, citrate, NO(3) (-), SO(4) (=), 2-n-heptyl or hydroxyquinoline-N-oxide (HOQNO), amytal or azide. The oxidation of these cellular pigments by fumarate was not inhibited by CN(-), CO, malonate, succinate, amytal, or HOQNO. Glucose and reduced diphosphopyridine nucleotide (DPNH), but not succinate, reduced the pigments in frozen-thawed cells previously exposed to air for 4 hr at room temperature. The results suggest that this cytochrome and flavoprotein form an electron transport system for fumarate reduction to succinate by DPNH generated by glycolysis, and that succinate is produced via CO(2) condensation with pyruvate or phosphoenolpyruvate and with oxalacetate, malate, and fumarate as intermediates. A pigment similar to cytochrome o (absorption maxima at 570, 555, and 416 mmu) was observed when reduced cells were treated with CO and compared to reduced cells, but there was no detectable cytochrome oxidase activity. The function of this pigment is obscure. No peroxidase or catalase activity was detected in either strain. Pyridine hemochromogens of both strains indicate one major heme, a protoheme-like pigment, with absorption in the alpha region maximum at 556 mmu. As B. ruminicola is one of the most numerous of rumen bacteria and ferments a wide variety of carbohydrates of importance in ruminant rations, cytochrome must be of importance in electron transport in rumen contents, a highly anaerobic environment.
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PMID:Cytochromelinked fermentation in Bacteroides ruminicola. 1400 Feb 91